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3  structures 1541  species 0  interactions 14205  sequences 168  architectures

Family: RINGv (PF12906)

Summary: RING-variant domain

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RING-variant domain Provide feedback

No Pfam abstract.

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011016

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [ PUBMED:10529348 , PUBMED:15963892 , PUBMED:15718139 , PUBMED:17210253 , PUBMED:12665246 ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [ PUBMED:11179890 ]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

The RING finger is a well characterised zinc finger which coordinates two zinc atoms in a cross-braced manner (see PROSITEDOC ). According to the pattern of cysteines and histidines three different subfamilies of RING finger can be defined. The classical RING finger (RING-HC) has a histidine at the fourth coordinating position and a cysteine at the fifth. In the RING-H2 variant, both the fourth and fifth positions are occupied by histidines. The RING-CH, which is very similar to the classical RING finger, differs from both of these variants in that it has a cys residue in the fourth position and a His in the fifth. Another difference between the RING-CH and the common RING variants is a somewhat longer peptide segment between the fourth and fifth zinc-coordinating residues. The RING-CH zinc finger has thus the same arrangement of cysteine and histidine (C4HC3) as the PHD zinc finger (see PROSITEDOC ) but it contains features (spacing between the cysteines and the histidine) characteristic of the genuine RING-finger (C3HC4) [ PUBMED:11641273 , PUBMED:12695663 ]. The RING-CH-type is an E3 ligase mainly found in proteins associated to membranes [ PUBMED:16873052 , PUBMED:17051211 ].

The solution structure of the RING-CH-type zinc finger of the herpesvirus Mir1 protein has shown that it is an outlying relative of the cellular RING finger domain family, with its polypeptide backbone much more closely resembling that of RING domains than PHD domains [ PUBMED:15465811 ]. The only real difference between the classic and variant RING domains, other than the alteration of zinc ligands, is the loss of the small beta-sheet found in RING domains and the replacement of one strand of this sheet with a single turn of helix. Some proteins that contains a RING-CH-type zinc finger are listed below:

  • Yeast Doa10/SSM4 ( SWISSPROT ). An E3 ligase essential for the endoplasmic reticulum associated degradation (ERAD), an ubiquitin-proteasome system responsible for the degradation of membrane and lumenal proteins of the endoplasmic reticulum.
  • Mammalian membrane-associated RING-CH 1 to 9 (MARCH1 to 9) proteins.
  • Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus) modulator of immune recognition 1 ( SWISSPROT ). An E3 ubiquitin-protein ligase which promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Bateman A
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 21
Number in full: 14205
Average length of the domain: 49.2 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 10.4 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 21.6 21.6
Noise cut-off 21.5 21.5
Model length: 48
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the RINGv domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044QTM8 View 3D Structure Click here
A0A044QYE3 View 3D Structure Click here
A0A044S1Y6 View 3D Structure Click here
A0A044VFI7 View 3D Structure Click here
A0A044VH96 View 3D Structure Click here
A0A077Z179 View 3D Structure Click here
A0A077Z828 View 3D Structure Click here
A0A077ZAP4 View 3D Structure Click here
A0A077ZJG3 View 3D Structure Click here
A0A0D2FC17 View 3D Structure Click here
A0A0D2G0P8 View 3D Structure Click here
A0A0D2GNL1 View 3D Structure Click here
A0A0H5S8K5 View 3D Structure Click here
A0A0H5SK87 View 3D Structure Click here
A0A0I9NB31 View 3D Structure Click here
A0A0K0E2B6 View 3D Structure Click here
A0A0K0E802 View 3D Structure Click here
A0A0K0EDT6 View 3D Structure Click here
A0A0K0EPT0 View 3D Structure Click here
A0A0K0EQP2 View 3D Structure Click here
A0A0K0ETI1 View 3D Structure Click here
A0A0K0JWM1 View 3D Structure Click here
A0A0N4UG68 View 3D Structure Click here
A0A0N7KDP5 View 3D Structure Click here
A0A0N7KJK3 View 3D Structure Click here
A0A0P0XBF7 View 3D Structure Click here
A0A0P0XVX8 View 3D Structure Click here
A0A0R0E898 View 3D Structure Click here
A0A0R0EBY7 View 3D Structure Click here
A0A0R0EEW7 View 3D Structure Click here
A0A0R0ELZ6 View 3D Structure Click here
A0A0R0GDU5 View 3D Structure Click here
A0A0R0GY62 View 3D Structure Click here
A0A0R0GZA9 View 3D Structure Click here
A0A0R0H6X3 View 3D Structure Click here
A0A0R0I151 View 3D Structure Click here
A0A0R0ITQ9 View 3D Structure Click here
A0A0R0K884 View 3D Structure Click here
A0A0R0KVD3 View 3D Structure Click here
A0A0R0LG38 View 3D Structure Click here